PDBsum entry: 1dbh

Gene regulation

PDB id: 1dbh

Contents

Protein chain

340 a.a. *

Waters ×69

* Residue conservation analysis

PDB id:

1dbh

Name:

Gene regulation

Title:

Dbl and pleckstrin homology domains from hsos1

Structure:

Protein (human sos 1). Chain: a. Fragment: dbl and pleckstrin homology domains. Synonym: son of sevenless protein. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.

Resolution:

2.30Å R-factor: 0.229 R-free: 0.269

Authors:

S.M.Soisson,J.Kuriyan

Key ref:

S.M.Soisson et al. (1998). Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein. Cell, 95, 259-268. PubMed id: 9790532 DOI: 10.1016/S0092-8674(00)81756-0

Date:

17-Dec-98 Release date: 23-Dec-98

Protein chain

Q07889  (SOS1_HUMAN) -  Son of sevenless homolog 1

Seq: 1333 a.a.

Struc: 340 a.a.

 Gene Ontology (GO) functional annotation 

• Cellular component: intracellular (1 term)
• Biological process: regulation of Rho protein signal transduction (1 term)
• Biochemical function: protein binding (2 terms)

DOI no: 10.1016/S0092-8674(00)81756-0

Cell 95:259-268 (1998)

PubMed id: 9790532

Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein.

S.M.Soisson, A.S.Nimnual, M.Uy, D.Bar-Sagi, J.Kuriyan.

ABSTRACT

Proteins containing Dbl homology (DH) domains activate Rho-family GTPases by functioning as specific guanine nucleotide exchange factors. All known DH domains have associated C-terminal pleckstrin homology (PH) domains that are implicated in targeting and regulatory functions. The crystal structure of a fragment of the human Son of sevenless protein containing the DH and PH domains has been determined at 2.3 A resolution. The entirely alpha-helical DH domain is unrelated in architecture to other nucleotide exchange factors. The active site of the DH domain, identified on the basis of sequence conservation and structural features, lies near the interface between the DH and PH domains. The structure suggests that ligation of the PH domain will be coupled structurally to the GTPase binding site.

Selected figure(s)

Figure 2.
Figure 2. Domain Structure of the Sos ProteinThe construct used for structure determination is depicted in color. The DH domain is colored blue, the PH domain is yellow, and the linker segment discussed in the text is colored red. The N domain, as described previously, is a structural component of the Ras exchange factor region ([4]). PxxP motifs are SH3-domain binding sites ( [2]).

Figure 3.
Figure 3. Ribbon Diagram of the Structure of the DH and PH Domains from SosAll ribbon diagrams were generated using the program RIBBONS ([7]). Coloring is as depicted in Figure 1; the DH domain is blue, the PH domain is yellow, and the linker segment is red. The conserved regions of the DH domain are labeled and colored as in Figure 1. Magenta, CR1; peach, CR2; olive green, CR3. Red ovals mark the amino- and carboxyl-terminal residues of the DH-PH domains (residues 198 and 550, respectively).

The above figures are reprinted by permission from Cell Press: Cell (1998, 95, 259-268) copyright 1998.

Figures were selected by an automated process.